N-15 and C-13 Group-Selective Techniques Extend the Scope of STD NMR Detection of Weak Host-Guest Interactions and Ligand Screening
Saturation transfer difference (STD) is a valuable tool for studying the binding of small molecules to large biomolecules and for obtaining detailed information on the binding epitopes. Here, we demonstrate that the proposed N-15/C-13 variants of group-selective, "GS-STD" experiments provi...
Elmentve itt :
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| Dokumentumtípus: | Cikk |
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Wiley-VCH Verlag GmbH & Co. KGaA
2010
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| Sorozat: | CHEMBIOCHEM
11 No. 15 |
| doi: | 10.1002/cbic.201000317 |
| mtmt: | 1452809 |
| Online Access: | http://publicatio.bibl.u-szeged.hu/10390 |
| Tartalmi kivonat: | Saturation transfer difference (STD) is a valuable tool for studying the binding of small molecules to large biomolecules and for obtaining detailed information on the binding epitopes. Here, we demonstrate that the proposed N-15/C-13 variants of group-selective, "GS-STD" experiments provide a powerful approach to mapping the binding epitope of a ligand even in the absence of efficient spin diffusion within the target protein. Therefore, these experimental variants broaden the scope of STD studies to smaller and/or more-dynamic targets. The STD spectra obtained in four different experimental setups (selective H-1 STD, N-15 GS-STD, C-13(Ar) and C-13(aliphatic) GS-STD approaches) revealed that the signal-intensity pattern of the difference spectra is affected by both the type and the spatial distribution of the excited "transmitter" atoms, as well as by the efficiency of the spin-diffusion-mediated magnetization transfer. The performance of the experiments is demonstrated on a system by using the lectin, galectin-1 and its carbohydrate ligand, lactose. |
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| Terjedelem/Fizikai jellemzők: | 2182-2187 |
| ISSN: | 1439-4227 |